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Journal articles

Academic literature on the topic 'Tamil Transcriptions'

Author: Grafiati

Published: 4 June 2021

Last updated: 3 February 2022

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Journal articles on the topic "Tamil Transcriptions"

1

Ito, Jun, Hidehiro Fukaki, Makoto Onoda, et al. "Auxin-dependent compositional change in Mediator in ARF7- and ARF19-mediated transcription." Proceedings of the National Academy of Sciences 113, no. 23 (2016): 6562–67. http://dx.doi.org/10.1073/pnas.1600739113.

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Mediator is a multiprotein complex that integrates the signals from transcription factors binding to the promoter and transmits them to achieve gene transcription. The subunits of Mediator complex reside in four modules: the head, middle, tail, and dissociable CDK8 kinase module (CKM). The head, middle, and tail modules form the core Mediator complex, and the association of CKM can modify the function of Mediator in transcription. Here, we show genetic and biochemical evidence that CKM-associated Mediator transmits auxin-dependent transcriptional repression in lateral root (LR) formation. The

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2

Georges, Sara A., W. Lee Kraus, Karolin Luger, Jennifer K. Nyborg, and Paul J. Laybourn. "p300-Mediated Tax Transactivation from Recombinant Chromatin: Histone Tail Deletion Mimics Coactivator Function." Molecular and Cellular Biology 22, no. 1 (2002): 127–37. http://dx.doi.org/10.1128/mcb.22.1.127-137.2002.

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ABSTRACT Efficient transcription of the human T-cell leukemia virus type 1 (HTLV-1) genome requires Tax, a virally encoded oncogenic transcription factor, in complex with the cellular transcription factor CREB and the coactivators p300/CBP. To examine Tax transactivation in vitro, we used a chromatin assembly system that included recombinant core histones. The addition of Tax, CREB, and p300 to the HTLV-1 promoter assembled into chromatin activated transcription several hundredfold. Chromatin templates selectively lacking amino-terminal histone tails demonstrated enhanced transcriptional activ

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3

Liu, Zhongle, and Lawrence C. Myers. "Fungal Mediator Tail Subunits Contain Classical Transcriptional Activation Domains." Molecular and Cellular Biology 35, no. 8 (2015): 1363–75. http://dx.doi.org/10.1128/mcb.01508-14.

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Classical activation domains within DNA-bound eukaryotic transcription factors make weak interactions with coactivator complexes, such as Mediator, to stimulate transcription. How these interactions stimulate transcription, however, is unknown. The activation of reporter genes by artificial fusion of Mediator subunits to DNA binding domains that bind to their promoters has been cited as evidence that the primary role of activators is simply to recruit Mediator. We have identified potent classical transcriptional activation domains in the C termini of several tail module subunits ofSaccharomyce

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4

McCulloch, Vicki, and Gerald S. Shadel. "Human Mitochondrial Transcription Factor B1 Interacts with the C-Terminal Activation Region of h-mtTFA and Stimulates Transcription Independently of Its RNA Methyltransferase Activity." Molecular and Cellular Biology 23, no. 16 (2003): 5816–24. http://dx.doi.org/10.1128/mcb.23.16.5816-5824.2003.

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ABSTRACT A significant advancement in understanding mitochondrial gene expression is the recent identification of two new human mitochondrial transcription factors, h-mtTFB1 and h-mtTFB2. Both proteins stimulate transcription in collaboration with the high-mobility group box transcription factor, h-mtTFA, and are homologous to rRNA methyltransferases. In fact, the dual-function nature of h-mtTFB1 was recently demonstrated by its ability to methylate a conserved rRNA substrate. Here, we demonstrate that h-mtTFB1 binds h-mtTFA both in HeLa cell mitochondrial extracts and in direct-binding assays

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5

Alff, Peter J., Nandini Sen, Elena Gorbunova, Irina N. Gavrilovskaya, and Erich R. Mackow. "The NY-1 Hantavirus Gn Cytoplasmic Tail Coprecipitates TRAF3 and Inhibits Cellular Interferon Responses by Disrupting TBK1-TRAF3 Complex Formation." Journal of Virology 82, no. 18 (2008): 9115–22. http://dx.doi.org/10.1128/jvi.00290-08.

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ABSTRACT Pathogenic hantaviruses replicate within human endothelial cells and cause two diseases, hemorrhagic fever with renal syndrome and hantavirus pulmonary syndrome. In order to replicate in endothelial cells pathogenic hantaviruses inhibit the early induction of beta interferon (IFN-β). Expression of the cytoplasmic tail of the pathogenic NY-1 hantavirus Gn protein is sufficient to inhibit RIG-I- and TBK1-directed IFN responses. The formation of TBK1-TRAF3 complexes directs IRF-3 phosphorylation, and both IRF-3 and NF-κB activation are required for transcription from the IFN-β promoter.

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6

Talbert, Paul B., and Steven Henikoff. "The Yin and Yang of Histone Marks in Transcription." Annual Review of Genomics and Human Genetics 22, no. 1 (2021): 147–70. http://dx.doi.org/10.1146/annurev-genom-120220-085159.

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Nucleosomes wrap DNA and impede access for the machinery of transcription. The core histones that constitute nucleosomes are subject to a diversity of posttranslational modifications, or marks, that impact the transcription of genes. Their functions have sometimes been difficult to infer because the enzymes that write and read them are complex, multifunctional proteins. Here, we examine the evidence for the functions of marks and argue that the major marks perform a fairly small number of roles in either promoting transcription or preventing it. Acetylations and phosphorylations on the histone

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7

Sims, Jennifer K., and Judd C. Rice. "PR-Set7 Establishes a Repressive trans-Tail Histone Code That Regulates Differentiation." Molecular and Cellular Biology 28, no. 14 (2008): 4459–68. http://dx.doi.org/10.1128/mcb.00410-08.

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ABSTRACT Posttranslational modifications of the DNA-associated histone proteins play fundamental roles in eukaryotic transcriptional regulation. We previously discovered a novel trans-tail histone code involving monomethylated histone H4 lysine 20 (H4K20) and H3 lysine 9 (H3K9); however, the mechanisms that establish this code and its function in transcription were unknown. In this report, we demonstrate that H3K9 monomethylation is dependent upon the PR-Set7 H4K20 monomethyltransferase but independent of its catalytic function, indicating that PR-Set7 recruits an H3K9 monomethyltransferase to

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8

WANG, Guannan, Jianyin LONG, Isao MATSUURA, Dongming HE, and Fang LIU. "The Smad3 linker region contains a transcriptional activation domain." Biochemical Journal 386, no. 1 (2005): 29–34. http://dx.doi.org/10.1042/bj20041820.

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Transforming growth factor-β (TGF-β)/Smads regulate a wide variety of biological responses through transcriptional regulation of target genes. Smad3 plays a key role in TGF-β/Smad-mediated transcriptional responses. Here, we show that the proline-rich linker region of Smad3 contains a transcriptional activation domain. When the linker region is fused to a heterologous DNA-binding domain, it activates transcription. We show that the linker region physically interacts with p300. The adenovirus E1a protein, which binds to p300, inhibits the transcriptional activity of the linker region, and overe

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9

Ryu, Hong-Yeoul, Dejian Zhao, Jianhui Li, Dan Su, and Mark Hochstrasser. "Histone sumoylation promotes Set3 histone-deacetylase complex-mediated transcriptional regulation." Nucleic Acids Research 48, no. 21 (2020): 12151–68. http://dx.doi.org/10.1093/nar/gkaa1093.

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Abstract Histones are substrates of the SUMO (small ubiquitin-like modifier) conjugation pathway. Several reports suggest histone sumoylation affects transcription negatively, but paradoxically, our genome-wide analysis shows the modification concentrated at many active genes. We find that trans-tail regulation of histone-H2B ubiquitylation and H3K4 di-methylation potentiates subsequent histone sumoylation. Consistent with the known control of the Set3 histone deacetylase complex (HDAC) by H3K4 di-methylation, histone sumoylation directly recruits the Set3 complex to both protein-coding and no

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10

Merrick, David, Kavita Mistry, Jingshing Wu, et al. "Polycystin-1 regulates bone development through an interaction with the transcriptional coactivator TAZ." Human Molecular Genetics 28, no. 1 (2018): 16–30. http://dx.doi.org/10.1093/hmg/ddy322.

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Abstract Polycystin-1 (PC1), encoded by the PKD1 gene that is mutated in the autosomal dominant polycystic kidney disease, regulates a number of processes including bone development. Activity of the transcription factor RunX2, which controls osteoblast differentiation, is reduced in Pkd1 mutant mice but the mechanism governing PC1 activation of RunX2 is unclear. PC1 undergoes regulated cleavage that releases its C-terminal tail (CTT), which translocates to the nucleus to modulate transcriptional pathways involved in proliferation and apoptosis. We find that the cleaved CTT of PC1 (PC1-CTT) sti

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